Photoaffinity labeling of functional states of the nicotinic acetylcholine receptor |
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Authors: | W. Oberthü r F. Hucho |
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Affiliation: | (1) Institut für Biochemie, Freie Universität Berlin, 1000 Berlin 33, West Germany;(2) Present address: Max-Planck-Institut für Biochemie, 8033 Martinsried, West Germany |
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Abstract: | The nicotinic acetycholine receptor was subjected to photoaffinity labeling in different conformational and functional states. The photolabel used was the ion-channel blocker [3H]-TPMP+. A procedure is described for isolating labeled -polypeptide chains from the receptor complex by preparative SDS-polyacrylamide gel electrophoresis. The photolabel was localized in the primary structure of the -chain. The site of labeling was found to be identical when photoaffinity labeling was performed in the resting, desensitized, or antagonist state, respectively. |
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Keywords: | nicotinic acetylcholine receptor photoaffinity labeling ion channel conformational states functional domains |
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